Protein Phosphatase 1 in association with Bud14 inhibits mitotic exit in Saccharomyces cerevisiae

Abstract Saccharomyces cerevisiae, also known as the budding yeast, orients and elongates its mitotic spindle along its polarity axis in order to segregate one copy of its genomic DNA to the daughter cell. When accurate positioning of the mitotic spindle fails, a surveillance mechanism, named the Sp...

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Bibliographic Details
Published inbioRxiv
Main Authors Kocakaplan, Dilara, Karabürk, Hüseyin, Dilege, Cansu, Kirdok, Idil, Erkan, Şeyma Nur, Ayse Koca Caydasi
Format Paper
LanguageEnglish
Published Cold Spring Harbor Cold Spring Harbor Laboratory Press 19.11.2020
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Summary:Abstract Saccharomyces cerevisiae, also known as the budding yeast, orients and elongates its mitotic spindle along its polarity axis in order to segregate one copy of its genomic DNA to the daughter cell. When accurate positioning of the mitotic spindle fails, a surveillance mechanism, named the Spindle Position Checkpoint (SPOC), prevents cells from exiting mitosis unless the spindle orientation is corrected. Mutants with a defective SPOC loss their genomic integrity, become multiploid and aneuploid. Thus, SPOC is a crucial checkpoint for the budding yeast. Yet, a comprehensive understanding of how the SPOC mechanism works is missing. In this study, we identified Bud14 as a novel checkpoint protein. We showed that the mitotic exit inhibitory function of Bud14 requires its association with the type 1 protein phosphatase, Glc7. Our data indicate that Glc7-Bud14 promotes dephosphorylation of the SPOC effector protein Bfa1. Our results support a model in which Glc7-Bud14 works parallel to the SPOC kinase Kin4 in inhibiting mitotic exit. Competing Interest Statement The authors have declared no competing interest.
DOI:10.1101/2020.08.30.273946